Analytical Data
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Gene name
CKLFSF7
- Application
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Alternative Names
CKLF-like MARVEL transmembrane domain-containing protein 7. Chemokine-like factor superfamily member 7
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96FZ5
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Expression Region
1-175aa
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AA Sequence
MSHGAGLVRTTCSSGSALGPGAGAAQPSASPLEGLLDLSYPRTHAALLKVAQMVTLLIAFICVRSSLWTNYSAYSYFEVVTICDLIMILAFYLVHLFRFYRVLTCISWPLSELLHYLIGTLLLLIASIVAASKSYNQSGLVAGAIFGFMATFLCMASIWLSYKISCVTQSTDAAV
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Molecular Weight
44.99 KDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
CKLFSF7, a member of the conserved kinesin-like protein family, has garnered interest due to its potential roles in cellular processes, particularly in mitosis and cytokinesis. Recent studies suggest that CKLFSF7 may influence spindle dynamics and chromosomal alignment, prompting investigations into its structure-function relationships. The protein's unique domain architecture, characterized by a kinesin motor domain, indicates a possible involvement in vesicle transport and organelle positioning within cells. As aberrations in these processes can lead to various diseases, including cancer, understanding CKLFSF7's functionality at the molecular level is paramount. Preliminary data have shown that overexpression or knockdown of CKLFSF7 can disrupt normal cell division, making it a candidate for further exploration in the context of tumorigenesis. Additionally, the potential regulatory mechanisms governing CKLFSF7 activity, including post-translational modifications, are under scrutiny. Researchers are employing various biochemical and cell biological approaches to elucidate the pathways in which CKLFSF7 participates, aiming to clarify its role as a critical player in maintaining cellular homeostasis. Overall, CKLFSF7's emerging significance in cell cycle regulation and its implications in pathological conditions highlight the necessity for comprehensive studies to fully understand its potential as a therapeutic target.
